Filtros : "ARANTES, GUILHERME MENEGON" "Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)" Removido: "BIOENERGÉTICA" Limpar

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  • Source: Journal of Chemical Information and Modeling. Unidade: IQ

    Subjects: ELÉTRONS, PEPTÍDEOS, PROTEÍNAS

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    • ABNT

      CAMILO, Sofia Rodrigues Guedes et al. Tunneling and nonadiabatic effects on a proton-coupled electron transfer model for the Qo site in cytochrome bc1. Journal of Chemical Information and Modeling, v. 61, p. 1840−1849, 2021Tradução . . Disponível em: https://doi.org/10.1021/acs.jcim.1c00008. Acesso em: 17 out. 2024.
    • APA

      Camilo, S. R. G., Curtolo, F., Galassi, V. V., & Arantes, G. M. (2021). Tunneling and nonadiabatic effects on a proton-coupled electron transfer model for the Qo site in cytochrome bc1. Journal of Chemical Information and Modeling, 61, 1840−1849. doi:10.1021/acs.jcim.1c00008
    • NLM

      Camilo SRG, Curtolo F, Galassi VV, Arantes GM. Tunneling and nonadiabatic effects on a proton-coupled electron transfer model for the Qo site in cytochrome bc1 [Internet]. Journal of Chemical Information and Modeling. 2021 ; 61 1840−1849.[citado 2024 out. 17 ] Available from: https://doi.org/10.1021/acs.jcim.1c00008
    • Vancouver

      Camilo SRG, Curtolo F, Galassi VV, Arantes GM. Tunneling and nonadiabatic effects on a proton-coupled electron transfer model for the Qo site in cytochrome bc1 [Internet]. Journal of Chemical Information and Modeling. 2021 ; 61 1840−1849.[citado 2024 out. 17 ] Available from: https://doi.org/10.1021/acs.jcim.1c00008
  • Source: Journal of Chemical Information and Modeling. Unidade: IQ

    Subjects: RESSONÂNCIA MAGNÉTICA NUCLEAR, PROTEÍNAS

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    • ABNT

      REIS, André Anversa Oliveira et al. Combining free energy simulations and NMR chemical-shift perturbation to identify transient cation−π contacts in proteins. Journal of Chemical Information and Modeling, v. 60, n. 2, p. 890–897, 2020Tradução . . Disponível em: https://doi.org/10.1021/acs.jcim.9b00859. Acesso em: 17 out. 2024.
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      Reis, A. A. O., Sayegh, R. S. R., Marana, S. R., & Arantes, G. M. (2020). Combining free energy simulations and NMR chemical-shift perturbation to identify transient cation−π contacts in proteins. Journal of Chemical Information and Modeling, 60( 2), 890–897. doi:10.1021/acs.jcim.9b00859
    • NLM

      Reis AAO, Sayegh RSR, Marana SR, Arantes GM. Combining free energy simulations and NMR chemical-shift perturbation to identify transient cation−π contacts in proteins [Internet]. Journal of Chemical Information and Modeling. 2020 ; 60( 2): 890–897.[citado 2024 out. 17 ] Available from: https://doi.org/10.1021/acs.jcim.9b00859
    • Vancouver

      Reis AAO, Sayegh RSR, Marana SR, Arantes GM. Combining free energy simulations and NMR chemical-shift perturbation to identify transient cation−π contacts in proteins [Internet]. Journal of Chemical Information and Modeling. 2020 ; 60( 2): 890–897.[citado 2024 out. 17 ] Available from: https://doi.org/10.1021/acs.jcim.9b00859
  • Source: Journal of Chemical Information and Modeling. Unidade: IQ

    Subjects: ÁTOMOS DE HIDROGÊNIO, OXIDAÇÃO

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    • ABNT

      CURTOLO, Felipe e ARANTES, Guilherme Menegon. Mechanisms for Flavin-mediated oxidation: hydride or hydrogen-atom transfer?. Journal of Chemical Information and Modeling, v. 60, n. 12, p. 6282–6287, 2020Tradução . . Disponível em: https://doi.org/10.1021/acs.jcim.0c00945. Acesso em: 17 out. 2024.
    • APA

      Curtolo, F., & Arantes, G. M. (2020). Mechanisms for Flavin-mediated oxidation: hydride or hydrogen-atom transfer? Journal of Chemical Information and Modeling, 60( 12), 6282–6287. doi:10.1021/acs.jcim.0c00945
    • NLM

      Curtolo F, Arantes GM. Mechanisms for Flavin-mediated oxidation: hydride or hydrogen-atom transfer? [Internet]. Journal of Chemical Information and Modeling. 2020 ; 60( 12): 6282–6287.[citado 2024 out. 17 ] Available from: https://doi.org/10.1021/acs.jcim.0c00945
    • Vancouver

      Curtolo F, Arantes GM. Mechanisms for Flavin-mediated oxidation: hydride or hydrogen-atom transfer? [Internet]. Journal of Chemical Information and Modeling. 2020 ; 60( 12): 6282–6287.[citado 2024 out. 17 ] Available from: https://doi.org/10.1021/acs.jcim.0c00945
  • Source: Journal of Chemical Information and Modeling. Unidade: IQ

    Subjects: HIDRÓLISE, FERRO, ENXOFRE

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      TEIXEIRA, Murilo Hoias et al. Modeling the hydrolysis of iron–sulfur clusters. Journal of Chemical Information and Modeling, v. 60, p. 653−660, 2020Tradução . . Disponível em: https://doi.org/10.1021/acs.jcim.9b00881. Acesso em: 17 out. 2024.
    • APA

      Teixeira, M. H., Curtolo, F., Camilo, S. R. G., Field, M. J., Zheng, P., Li, H., & Arantes, G. M. (2020). Modeling the hydrolysis of iron–sulfur clusters. Journal of Chemical Information and Modeling, 60, 653−660. doi:10.1021/acs.jcim.9b00881
    • NLM

      Teixeira MH, Curtolo F, Camilo SRG, Field MJ, Zheng P, Li H, Arantes GM. Modeling the hydrolysis of iron–sulfur clusters [Internet]. Journal of Chemical Information and Modeling. 2020 ; 60 653−660.[citado 2024 out. 17 ] Available from: https://doi.org/10.1021/acs.jcim.9b00881
    • Vancouver

      Teixeira MH, Curtolo F, Camilo SRG, Field MJ, Zheng P, Li H, Arantes GM. Modeling the hydrolysis of iron–sulfur clusters [Internet]. Journal of Chemical Information and Modeling. 2020 ; 60 653−660.[citado 2024 out. 17 ] Available from: https://doi.org/10.1021/acs.jcim.9b00881
  • Source: Abstracts. Conference titles: Congresso da Sociedade Brasileira de Biofísica. Unidade: IQ

    Subjects: CATÁLISE, ENZIMAS

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      CURTOLO, Felipe e ARANTES, Guilherme Menegon. Influence of active site flexibility in enzymatic succinate dehydrogenation. 2019, Anais.. Santos: Sociedade Brasileira de Biofísica/SBBf, 2019. . Acesso em: 17 out. 2024.
    • APA

      Curtolo, F., & Arantes, G. M. (2019). Influence of active site flexibility in enzymatic succinate dehydrogenation. In Abstracts. Santos: Sociedade Brasileira de Biofísica/SBBf.
    • NLM

      Curtolo F, Arantes GM. Influence of active site flexibility in enzymatic succinate dehydrogenation. Abstracts. 2019 ;[citado 2024 out. 17 ]
    • Vancouver

      Curtolo F, Arantes GM. Influence of active site flexibility in enzymatic succinate dehydrogenation. Abstracts. 2019 ;[citado 2024 out. 17 ]
  • Source: Biochimica et Biophysica Acta-Bioenergetics. Unidade: IQ

    Subjects: HIDRATAÇÃO, PROTEÍNAS, MOLÉCULA

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      TEIXEIRA, Murilo Hoias e ARANTES, Guilherme Menegon. Balanced internal hydration discriminates substrate binding to respiratory complex I. Biochimica et Biophysica Acta-Bioenergetics, v. 1860, n. 7, p. 541-548, 2019Tradução . . Disponível em: https://doi.org/10.1016/j.bbabio.2019.05.004. Acesso em: 17 out. 2024.
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      Teixeira, M. H., & Arantes, G. M. (2019). Balanced internal hydration discriminates substrate binding to respiratory complex I. Biochimica et Biophysica Acta-Bioenergetics, 1860( 7), 541-548. doi:10.1016/j.bbabio.2019.05.004
    • NLM

      Teixeira MH, Arantes GM. Balanced internal hydration discriminates substrate binding to respiratory complex I [Internet]. Biochimica et Biophysica Acta-Bioenergetics. 2019 ; 1860( 7): 541-548.[citado 2024 out. 17 ] Available from: https://doi.org/10.1016/j.bbabio.2019.05.004
    • Vancouver

      Teixeira MH, Arantes GM. Balanced internal hydration discriminates substrate binding to respiratory complex I [Internet]. Biochimica et Biophysica Acta-Bioenergetics. 2019 ; 1860( 7): 541-548.[citado 2024 out. 17 ] Available from: https://doi.org/10.1016/j.bbabio.2019.05.004
  • Source: Abstracts. Conference titles: Congresso da Sociedade Brasileira de Biofísica. Unidade: IQ

    Subjects: MODELAGEM MOLECULAR, PROTEÍNAS

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    • ABNT

      TEIXEIRA, Murilo Hoias e ARANTES, Guilherme Menegon. Calculation of redox potentials for iron-sulfur proteins. 2019, Anais.. Santos: Sociedade Brasileira de Biofísica/SBBf, 2019. . Acesso em: 17 out. 2024.
    • APA

      Teixeira, M. H., & Arantes, G. M. (2019). Calculation of redox potentials for iron-sulfur proteins. In Abstracts. Santos: Sociedade Brasileira de Biofísica/SBBf.
    • NLM

      Teixeira MH, Arantes GM. Calculation of redox potentials for iron-sulfur proteins. Abstracts. 2019 ;[citado 2024 out. 17 ]
    • Vancouver

      Teixeira MH, Arantes GM. Calculation of redox potentials for iron-sulfur proteins. Abstracts. 2019 ;[citado 2024 out. 17 ]
  • Source: Abstracts. Conference titles: Congresso da Sociedade Brasileira de Biofísica. Unidade: IQ

    Subjects: BIOLOGIA MOLECULAR, PROTEÍNAS

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      REIS, André Anversa Oliveira et al. Molecular recognition by CDC25B phosphatases. 2019, Anais.. Santos: Sociedade Brasileira de Biofísica/SBBf, 2019. . Acesso em: 17 out. 2024.
    • APA

      Reis, A. A. O., Sayegh, R. S. R., Marana, S. R., & Arantes, G. M. (2019). Molecular recognition by CDC25B phosphatases. In Abstracts. Santos: Sociedade Brasileira de Biofísica/SBBf.
    • NLM

      Reis AAO, Sayegh RSR, Marana SR, Arantes GM. Molecular recognition by CDC25B phosphatases. Abstracts. 2019 ;[citado 2024 out. 17 ]
    • Vancouver

      Reis AAO, Sayegh RSR, Marana SR, Arantes GM. Molecular recognition by CDC25B phosphatases. Abstracts. 2019 ;[citado 2024 out. 17 ]
  • Source: RSC Advances. Unidade: IQ

    Subjects: LIPÍDEOS, MOLÉCULA

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      TEIXEIRA, Murilo Hoias e ARANTES, Guilherme Menegon. Effects of lipid composition on membrane distribution and permeability of natural quinones. RSC Advances, v. 9 p. 16892-16899, 2019Tradução . . Disponível em: https://doi.org/10.1039/c9ra01681. Acesso em: 17 out. 2024.
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      Teixeira, M. H., & Arantes, G. M. (2019). Effects of lipid composition on membrane distribution and permeability of natural quinones. RSC Advances, 9 p. 16892-16899. doi:10.1039/c9ra01681
    • NLM

      Teixeira MH, Arantes GM. Effects of lipid composition on membrane distribution and permeability of natural quinones [Internet]. RSC Advances. 2019 ; 9 p. 16892-16899[citado 2024 out. 17 ] Available from: https://doi.org/10.1039/c9ra01681
    • Vancouver

      Teixeira MH, Arantes GM. Effects of lipid composition on membrane distribution and permeability of natural quinones [Internet]. RSC Advances. 2019 ; 9 p. 16892-16899[citado 2024 out. 17 ] Available from: https://doi.org/10.1039/c9ra01681
  • Source: PLOS ONE. Unidade: IQ

    Subjects: GLICOSÍDEOS, MUTAÇÃO

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      SOUZA, Valquiria Pianheri et al. Mutations close to a hub residue affect the distant active site of a GH1 beta-glucosidase. PLOS ONE, v. 13, n. 6, p. 1-12 art. e0198696, 2018Tradução . . Disponível em: https://doi.org/10.1371/journal.pone.0198696. Acesso em: 17 out. 2024.
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      Souza, V. P., Ikegami, C. M., Arantes, G. M., & Marana, S. R. (2018). Mutations close to a hub residue affect the distant active site of a GH1 beta-glucosidase. PLOS ONE, 13( 6), 1-12 art. e0198696. doi:10.1371/journal.pone.0198696
    • NLM

      Souza VP, Ikegami CM, Arantes GM, Marana SR. Mutations close to a hub residue affect the distant active site of a GH1 beta-glucosidase [Internet]. PLOS ONE. 2018 ; 13( 6): 1-12 art. e0198696.[citado 2024 out. 17 ] Available from: https://doi.org/10.1371/journal.pone.0198696
    • Vancouver

      Souza VP, Ikegami CM, Arantes GM, Marana SR. Mutations close to a hub residue affect the distant active site of a GH1 beta-glucosidase [Internet]. PLOS ONE. 2018 ; 13( 6): 1-12 art. e0198696.[citado 2024 out. 17 ] Available from: https://doi.org/10.1371/journal.pone.0198696

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